AC   MF_03181;
DC   Protein; auto
TR   HAMAP; MF_03181; -; 1; level=0
XX
Names: PAN3
XX
ID   PAN3
DE   RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3;
DE   AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease;
DE   AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3;
DE            Short=PAN deadenylation complex subunit 3;
GN   Name=PAN3;
XX
case <OC:Metazoa>
CC   -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC       deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC       involved in general and miRNA-mediated mRNA turnover. PAN specifically
CC       shortens poly(A) tails of RNA and the activity is stimulated by
CC       poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid
CC       degradation of the shortened mRNA tails by the CCR4-NOT complex.
CC       Deadenylated mRNAs are then degraded by two alternative mechanisms,
CC       namely exosome-mediated 3'-5' exonucleolytic degradation, or
CC       deadenlyation-dependent mRNA decaping and subsequent 5'-3'
CC       exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator
CC       for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its
CC       interaction with RNA and PABP, and to miRNA targets via its interaction
CC       with GW182 family proteins.
else case <OC:Fungi>
CC   -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC       deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC       involved in mRNA turnover. PAN specifically shortens poly(A) tails of
CC       RNA and the activity is stimulated by poly(A)-binding protein
CC       @gn(PAB1). PAN deadenylation is followed by rapid degradation of the
CC       shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are
CC       then degraded by two alternative mechanisms, namely exosome-mediated
CC       3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA
CC       decaping and subsequent 5'-3' exonucleolytic degradation by @gn(XRN1).
CC       May also be involved in post-transcriptional maturation of mRNA poly(A)
CC       tails. @gn(PAN3) acts as a positive regulator for PAN activity,
CC       recruiting the catalytic subunit @gn(PAN2) to mRNA via its interaction
CC       with RNA and with @gn(PAB1).
else
CC   -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC       deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC       involved in mRNA turnover. PAN specifically shortens poly(A) tails of
CC       RNA and the activity is stimulated by poly(A)-binding protein (PABP).
CC       PAN deadenylation is followed by rapid degradation of the shortened
CC       mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then
CC       degraded by two alternative mechanisms, namely exosome-mediated 3'-5'
CC       exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC       and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a
CC       positive regulator for PAN activity, recruiting the catalytic subunit
CC       PAN2 to mRNA via its interaction with RNA and PABP.
end case
case <OC:Vertebrata>
CC   -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit
CC       @gn(PAN2) to form the poly(A)-nuclease (PAN) deadenylation complex.
CC       Interacts (via PAM-2 motif) with poly(A)-binding protein @gn(PABPC1)
CC       (via PABC domain), conferring substrate specificity of the enzyme
CC       complex. Interacts with the GW182 family proteins @gn(TNRC6A),
CC       @gn(TNRC6B) and @gn(TNRC6C).
else case <OC:Metazoa>
CC   -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit
CC       @gn(PAN2) to form the poly(A)-nuclease (PAN) deadenylation complex.
CC       Interacts (via PAM-2 motif) with poly(A)-binding protein (via PABC
CC       domain), conferring substrate specificity of the enzyme complex.
else case <OC:Fungi>
CC   -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit
CC       @gn(PAN2) to form the poly(A)-nuclease (PAN) deadenylation complex.
CC       Interacts (via PAM-2 motif) with poly(A)-binding protein @gn(PAB1) (via
CC       PABC domain), conferring substrate specificity of the enzyme complex.
else
CC   -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2
CC       to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts
CC       (via PAM-2 motif) with poly(A)-binding protein (via PABC domain),
CC       conferring substrate specificity of the enzyme complex.
end case
case <OC:Metazoa>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC   -!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain is
CC       predicted to be catalytically inactive because some of the residues
CC       important for catalytic activity are substituted and it lacks the
CC       equivalent of the binding site for a peptide substrate. However, it has
CC       retained an ATP-binding site and ATP-binding is required for mRNA
CC       degradation, stimulating the activity of the @gn(PAN2) nuclease in
CC       vitro. The nucleotide-binding site is juxtaposed to the RNase active
CC       site of @gn(PAN2) in the complex and may actually bind nucleosides of a
CC       poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active
CC       site of the deadenylase and thus increasing the efficiency with which
CC       this distributive enzyme degrades oligo(A) RNAs.
CC   -!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal
CC       knob domain (CK) form a structural unit (PKC) that forms an extensive
CC       high-affinity interaction surface for @gn(PAN2).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
XX
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 0-1; trigger=no
DR   PROSITE; PS50103; ZF_C3H1; 0-1; trigger=yes
DR   Pfam; PF00069; Pkinase; 1; trigger=no
XX
KW   ATP-binding
KW   Coiled coil
KW   Cytoplasm
KW   mRNA processing
KW   Nucleotide-binding
XX
case <OC:Metazoa>
GO   GO:0000932; C:P-body
GO   GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly
else
GO   GO:0005737; C:cytoplasm
end case
case <Feature:PS50103>
GO   GO:0046872; F:metal ion binding
end case
GO   GO:0031251; C:PAN complex
GO   GO:0005524; F:ATP binding
GO   GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
GO   GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening
XX
FT   From: PAN3_HUMAN (Q58A45)
case <OC:Mammalia>
FT   MOTIF           284..299
FT                   /note="PABPC-interacting motif-2 (PAM-2)"
FT   Optional; Condition: x(9)-F-x-P-x(4)
end case
FT   From: PAN3_YEAST (P36102)
case <OC:Fungi>
FT   MOTIF           143..163
FT                   /note="PABPC-interacting motif-2 (PAM-2)"
FT   Optional; Condition: x(13)-F-x-P-x(5)
end case
FT   REGION          275..548
FT                   /note="Pseudokinase domain"
FT   REGION          588..Cter
FT                   /note="Knob domain"
FT   COILED          549..587
FT   From: PAN3_NEUCR (Q7SDP4)
FT   BINDING         352..359
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DE]-[YF]-[HYF]-[PA]-x(3)-[ST]
FT   BINDING         412..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: x-K
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [RK]
XX
Size: 589-887;
Related: None;
Template: Q7SDP4; P36102; Q58A45; Q95RR8; G0S0Y3;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in SCHPO
Plasmid: None
Comments: None
XX
# Revision 1.8 2022/11/19
//